ID   MEP6_ARTOC              Reviewed;         270 AA.
AC   C5FQJ4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Extracellular metalloprotease MCYG_04966;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=MCYG_04966;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Plays a pivotal role as a pathogenicity
CC       determinant during infections and contributes to the ability of the
CC       pathogen to persist within the mammalian host (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; DS995704; EEQ32147.1; -; Genomic_DNA.
DR   RefSeq; XP_002847229.1; XM_002847183.1.
DR   AlphaFoldDB; C5FQJ4; -.
DR   SMR; C5FQJ4; -.
DR   STRING; 554155.C5FQJ4; -.
DR   EnsemblFungi; EEQ32147; EEQ32147; MCYG_04966.
DR   GeneID; 9223835; -.
DR   eggNOG; ENOG502RYKG; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   OMA; MTMNYMD; -.
DR   OrthoDB; 1569419at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04275; ZnMc_pappalysin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   Pfam; PF05572; Peptidase_M43; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..270
FT                   /note="Extracellular metalloprotease MCYG_04966"
FT                   /id="PRO_0000407212"
FT   REGION          208..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        221..247
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  28775 MW;  B07979DB7B507707 CRC64;
     MRLSLFLSGL AAAGSIVSAE RTCGAVPPRG YEKEFSEAFA ALGPEATSDL TAGITIDTYL
     HVLTSGTTGN IPDSQLQAQI NAMNQHYGPS GVQFRLVKAT RTNNANWASG RDEAGMKSAL
     HMGTYSSLNI YFIPNLSSGL LGICYFPRAN PSQTTITMDG CMVRSGTVPG GETTNYNQGK
     TATHEVGHFL GLYHVFSENG SCVDADMVAD TPPQSKKTSG CPNSQDSCPG GGVDSIHNYM
     DYSYDVCMNQ FTRGQASRIA QAWQAFRAGH